Role of High-Fidelity Escherichia coli DNA Polymerase I in Replication Bypass of a Deoxyadenosine DNA-Peptide Cross-Link

Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commer...

Full description

Saved in:
Bibliographic Details
Published inJournal of Bacteriology Vol. 193; no. 15; pp. 3815 - 3821
Main Authors YAMANAKA, Kinrin, MINKO, Irina G, FINKEL, Steven E, GOODMAN, Myron F, STEPHEN LLOYD, R
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.08.2011
Subjects
Bacteriology
Biological and medical sciences
Cells
Cross-Linking Reagents - chemistry
Deoxyadenosines - chemistry
Deoxyadenosines - genetics
DNA Adducts - chemistry
DNA Adducts - genetics
DNA Damage
DNA Polymerase I - genetics
DNA Polymerase I - metabolism
DNA Repair
DNA Replication
DNA, Bacterial - chemistry
DNA, Bacterial - genetics
DNA, Single-Stranded - genetics
E coli
Escherichia coli - enzymology
Escherichia coli - genetics
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Fundamental and applied biological sciences. Psychology
Genetics and Molecular Biology
Microbiology
Miscellaneous
Peptides
Peptides - chemistry
Nucleotidyltransferases
Peptides
Enzyme
Transferases
Escherichia coli
Bacteria
Replication
DNA-directed DNA polymerase
Enterobacteriaceae
Online AccessGet full text

Cover

Abstract Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JB .asm.org, visit: JB       
AbstractList Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JB .asm.org, visit: JB       
Reaction of bifunctional electrophiles with DNA in the presence of peptides can result in DNA-peptide cross-links. In particular, the linkage can be formed in the major groove of DNA via the exocyclic amino group of adenine ( N 6 -dA). We previously demonstrated that an A family human polymerase, Pol ν, can efficiently and accurately synthesize DNA past N 6 -dA-linked peptides. Based on these results, we hypothesized that another member of that family, Escherichia coli polymerase I (Pol I), may also be able to bypass these large major groove DNA lesions. To test this, oligodeoxynucleotides containing a site-specific N 6 -dA dodecylpeptide cross-link were created and utilized for in vitro DNA replication assays using E. coli DNA polymerases. The results showed that Pol I and Pol II could efficiently and accurately bypass this adduct, while Pol III replicase, Pol IV, and Pol V were strongly inhibited. In addition, cellular studies were conducted using E. coli strains that were either wild type or deficient in all three DNA damage-inducible polymerases, i.e., Pol II, Pol IV, and Pol V. When single-stranded DNA vectors containing a site-specific N 6 -dA dodecylpeptide cross-link were replicated in these strains, the efficiencies of replication were comparable, and in both strains, intracellular bypass of the lesion occurred in an error-free manner. Collectively, these findings demonstrate that despite its constrained active site, Pol I can catalyze DNA synthesis past N 6 -dA-linked peptide cross-links and is likely to play an essential role in cellular bypass of large major groove DNA lesions.
Reaction of bifunctional electrophiles with DNA in the presence of peptides can result in DNA-peptide cross-links. In particular, the linkage can be formed in the major groove of DNA via the exocyclic amino group of adenine (N⁶-dA). We previously demonstrated that an A family human polymerase, Pol ν, can efficiently and accurately synthesize DNA past N⁶-dA-linked peptides. Based on these results, we hypothesized that another member of that family, Escherichia coli polymerase I (Pol I), may also be able to bypass these large major groove DNA lesions. To test this, oligodeoxynucleotides containing a site-specific N⁶-dA dodecylpeptide cross-link were created and utilized for in vitro DNA replication assays using E. coli DNA polymerases. The results showed that Pol I and Pol II could efficiently and accurately bypass this adduct, while Pol III replicase, Pol IV, and Pol V were strongly inhibited. In addition, cellular studies were conducted using E. coli strains that were either wild type or deficient in all three DNA damage-inducible polymerases, i.e., Pol II, Pol IV, and Pol V. When single-stranded DNA vectors containing a site-specific N⁶-dA dodecylpeptide cross-link were replicated in these strains, the efficiencies of replication were comparable, and in both strains, intracellular bypass of the lesion occurred in an error-free manner. Collectively, these findings demonstrate that despite its constrained active site, Pol I can catalyze DNA synthesis past N⁶-dA-linked peptide cross-links and is likely to play an essential role in cellular bypass of large major groove DNA lesions.
Reaction of bifunctional electrophiles with DNA in the presence of peptides can result in DNA-peptide cross-links. In particular, the linkage can be formed in the major groove of DNA via the exocyclic amino group of adenine (N...-dA). We previously demonstrated that an A family human polymerase, Pol ..., can efficiently and accurately synthesize DNA past N...-dA-linked peptides. Based on these results, we hypothesized that another member of that family, Escherichia coli polymerase I (Pol I), may also be able to bypass these large major groove DNA lesions. To test this, oligodeoxynucleotides containing a site-specific N...-dA dodecylpeptide cross-link were created and utilized for in vitro DNA replication assays using E. coli DNA polymerases. The results showed that Pol I and Pol II could efficiently and accurately bypass this adduct, while Pol III replicase, Pol IV, and Pol V were strongly inhibited. In addition, cellular studies were conducted using E. coli strains that were either wild type or deficient in all three DNA damage-inducible polymerases, i.e., Pol II, Pol IV, and Pol V. When single-stranded DNA vectors containing a site-specific N...-dA dodecylpeptide cross-link were replicated in these strains, the efficiencies of replication were comparable, and in both strains, intracellular bypass of the lesion occurred in an error-free manner. Collectively, these findings demonstrate that despite its constrained active site, Pol I can catalyze DNA synthesis past N...-dA-linked peptide cross-links and is likely to play an essential role in cellular bypass of large major groove DNA lesions. (ProQuest: ... denotes formulae/symbols omitted.)
ABSTRACT Reaction of bifunctional electrophiles with DNA in the presence of peptides can result in DNA-peptide cross-links. In particular, the linkage can be formed in the major groove of DNA via the exocyclic amino group of adenine ( N 6 -dA). We previously demonstrated that an A family human polymerase, Pol ν, can efficiently and accurately synthesize DNA past N 6 -dA-linked peptides. Based on these results, we hypothesized that another member of that family, Escherichia coli polymerase I (Pol I), may also be able to bypass these large major groove DNA lesions. To test this, oligodeoxynucleotides containing a site-specific N 6 -dA dodecylpeptide cross-link were created and utilized for in vitro DNA replication assays using E. coli DNA polymerases. The results showed that Pol I and Pol II could efficiently and accurately bypass this adduct, while Pol III replicase, Pol IV, and Pol V were strongly inhibited. In addition, cellular studies were conducted using E. coli strains that were either wild type or deficient in all three DNA damage-inducible polymerases, i.e., Pol II, Pol IV, and Pol V. When single-stranded DNA vectors containing a site-specific N 6 -dA dodecylpeptide cross-link were replicated in these strains, the efficiencies of replication were comparable, and in both strains, intracellular bypass of the lesion occurred in an error-free manner. Collectively, these findings demonstrate that despite its constrained active site, Pol I can catalyze DNA synthesis past N 6 -dA-linked peptide cross-links and is likely to play an essential role in cellular bypass of large major groove DNA lesions.
Author R. Stephen Lloyd
Steven E. Finkel
Myron F. Goodman
Irina G. Minko
Kinrin Yamanaka
Author_xml – sequence: 1
  givenname: Kinrin
  surname: YAMANAKA
  fullname: YAMANAKA, Kinrin
  organization: Center for Research on Occupational and Environmental Toxicology, Oregon Health & Science University, Portland, Oregon 97239, United States
– sequence: 2
  givenname: Irina G
  surname: MINKO
  fullname: MINKO, Irina G
  organization: Center for Research on Occupational and Environmental Toxicology, Oregon Health & Science University, Portland, Oregon 97239, United States
– sequence: 3
  givenname: Steven E
  surname: FINKEL
  fullname: FINKEL, Steven E
  organization: Department of Biological Sciences, Oregon Health & Science University, Portland, Oregon 97239, United States
– sequence: 4
  givenname: Myron F
  surname: GOODMAN
  fullname: GOODMAN, Myron F
  organization: Department of Biological Sciences, Oregon Health & Science University, Portland, Oregon 97239, United States
– sequence: 5
  givenname: R
  surname: STEPHEN LLOYD
  fullname: STEPHEN LLOYD, R
  organization: Center for Research on Occupational and Environmental Toxicology, Oregon Health & Science University, Portland, Oregon 97239, United States
BackLink http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24404536$$DView record in Pascal Francis
https://www.ncbi.nlm.nih.gov/pubmed/21622737$$D View this record in MEDLINE/PubMed
BookMark eNpVkUFv1DAQhS1URLeFE3dkIXFCKXZsJ84FqbttaasVVBWcLceZNF6ydrCz0Px7HLq0cBrJ8_nNe3pH6MB5Bwi9puSE0lx-uF6eECoEySh5hhaUFGUmJcsP0IKQnGYVrdghOopxQwjlXOQv0GFOizwvWblA97e-B-xbfGnvuuzCNtDbccLn0XQQrOmsxsb3Fp99PsU3vp-2EHQEfIWtw7cw9Nbo0XqHl9OgY5yFND4Dfz_pBpyP1sH8NbuBYUzaeBV8jNnauu8v0fNW9xFe7ecx-nZx_nV1ma2_fLpana4zwws-ZibPuaw1raqaNDwF0ryuZNMYIkVJTVNA2zQpFdS0YKIAKdpakAII0LZsZMWO0ccH3WFXb6Ex4MagezUEu9VhUl5b9f_G2U7d-Z-KUV4KIpLA271A8D92EEe18bvgkmcly4qxglTzlfcPkJkDBmgfD1Ci5pbU9VL9aSk9JPrNv54e2b-1JODdHtDR6L4N2hkbnzjOCResePLWpfZ-2QBKx63a1Cp1rqhQTFLBfgMdM6bw
CODEN JOBAAY
CitedBy_id crossref_primary_10_1016_j_mrfmmm_2020_111702
crossref_primary_10_3390_ijms241310877
crossref_primary_10_1111_febs_14290
crossref_primary_10_1371_journal_pone_0198480
crossref_primary_10_1534_genetics_113_151837
crossref_primary_10_1074_jbc_M114_613638
crossref_primary_10_1021_bc400018u
crossref_primary_10_1016_j_mrfmmm_2011_12_004
crossref_primary_10_1128_AAC_01415_16
crossref_primary_10_1016_j_jbc_2021_101124
crossref_primary_10_1128_AAC_01577_18
crossref_primary_10_1093_nar_gkad423
crossref_primary_10_1128_JB_00201_18
crossref_primary_10_1021_cb5001795
crossref_primary_10_1016_j_jbc_2021_100444
crossref_primary_10_1073_pnas_1703066114
crossref_primary_10_1074_jbc_M114_561563
crossref_primary_10_1074_jbc_M113_458802
Cites_doi 10.1016/S0021-9258(19)69488-3
10.1016/j.mrfmmm.2007.08.001
10.1021/tx800174a
10.1021/tx00045a014
10.1074/jbc.M212012200
10.1016/S0021-9258(19)49928-6
10.1016/0076-6879(95)62004-4
10.1021/tx9000489
10.1021/bi980401f
10.1074/jbc.271.18.10767
10.1016/S0065-3233(04)71011-6
10.1021/bi100364f
10.1021/bi048244+
10.1093/emboj/19.23.6536
10.1016/S0021-9258(18)99166-0
10.1006/jmbi.2001.4619
10.1146/annurev.biochem.71.083101.124707
10.1074/jbc.M204826200
10.1021/bi0478805
10.1073/pnas.042700399
10.1016/j.mrrev.2004.11.003
10.1371/journal.pone.0010862
10.1074/jbc.270.22.13348
10.1128/jb.179.7.2109-2115.1997
10.1093/nar/23.8.1398
10.1021/tx990167+
10.1038/35010020
10.1073/pnas.092269199
10.1021/bi00126a006
10.1126/science.7681219
10.1128/MMBR.62.2.434-464.1998
10.1021/tx900449u
ContentType Journal Article
Copyright 2015 INIST-CNRS
Copyright American Society for Microbiology Aug 2011
Copyright © 2011, American Society for Microbiology. All Rights Reserved. 2011 American Society for Microbiology
Copyright_xml – notice: 2015 INIST-CNRS
– notice: Copyright American Society for Microbiology Aug 2011
– notice: Copyright © 2011, American Society for Microbiology. All Rights Reserved. 2011 American Society for Microbiology
DBID IQODW
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7QL
7TM
7U9
8FD
C1K
FR3
H94
M7N
P64
RC3
5PM
DOI 10.1128/JB.01550-10
DatabaseName Pascal-Francis
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
Bacteriology Abstracts (Microbiology B)
Nucleic Acids Abstracts
Virology and AIDS Abstracts
Technology Research Database
Environmental Sciences and Pollution Management
Engineering Research Database
AIDS and Cancer Research Abstracts
Algology Mycology and Protozoology Abstracts (Microbiology C)
Biotechnology and BioEngineering Abstracts
Genetics Abstracts
PubMed Central (Full Participant titles)
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Genetics Abstracts
Virology and AIDS Abstracts
Technology Research Database
Bacteriology Abstracts (Microbiology B)
Algology Mycology and Protozoology Abstracts (Microbiology C)
Nucleic Acids Abstracts
AIDS and Cancer Research Abstracts
Engineering Research Database
Biotechnology and BioEngineering Abstracts
Environmental Sciences and Pollution Management
DatabaseTitleList

MEDLINE
Genetics Abstracts
CrossRef
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 1067-8832
1098-5530
EndPage 3821
ExternalDocumentID 2408237221
10_1128_JB_01550_10
21622737
24404536
jb_193_15_3815
Genre Research Support, U.S. Gov't, Non-P.H.S
Research Support, U.S. Gov't, P.H.S
Journal Article
Research Support, N.I.H., Extramural
GrantInformation_xml – fundername: NIEHS NIH HHS
  grantid: R01 ES012259
– fundername: NIGMS NIH HHS
  grantid: R01 GM021422
– fundername: NIEHS NIH HHS
  grantid: P01 ES005355
– fundername: NCI NIH HHS
  grantid: R01 CA106858
– fundername: NIEHS NIH HHS
  grantid: ES012259
– fundername: NCI NIH HHS
  grantid: P01 CA160032
– fundername: NIGMS NIH HHS
  grantid: R37 GM021422
– fundername: NIEHS NIH HHS
  grantid: ES05355
– fundername: NCI NIH HHS
  grantid: CA106858
– fundername: NIGMS NIH HHS
  grantid: GM21422
GroupedDBID ---
-DZ
-~X
.55
.GJ
08R
0R~
186
18M
1VV
29J
2WC
39C
3O-
4.4
53G
5GY
5RE
5VS
79B
85S
8WZ
9M8
A6W
AAUGY
ABPPZ
ABPTK
ABTAH
ACGFO
ACGOD
ACNCT
ACPRK
ADBBV
AENEX
AFDAS
AFFDN
AFFNX
AFMIJ
AFRAH
AGCDD
AI.
AIDAL
AJUXI
ALMA_UNASSIGNED_HOLDINGS
AOIJS
BAWUL
BKOMP
BTFSW
C1A
CJ0
CS3
DIK
DU5
E3Z
EBS
EJD
F20
F5P
FRP
GX1
H13
HYE
HZ~
IH2
IQODW
KQ8
L7B
MVM
NHB
O9-
OHT
OK1
P-S
P2P
PQQKQ
QZG
RHF
RHI
RNS
RPM
RSF
RXW
TAE
TAF
TR2
UCJ
UHB
UKR
UPT
VH1
VQA
W8F
WH7
WHG
WOQ
X7M
XFK
Y6R
YQT
YR2
YZZ
ZA5
ZCA
ZCG
ZGI
ZXP
ZY4
~02
~KM
AGVNZ
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7QL
7TM
7U9
8FD
C1K
FR3
H94
M7N
P64
RC3
5PM
ID FETCH-LOGICAL-c464t-c2248ba199b0d4002a4b98ddc08571cd6efdd445eb16356e85fb506e0e1f7d893
IEDL.DBID RPM
ISSN 0021-9193
IngestDate Tue Sep 17 21:26:46 EDT 2024
Thu Oct 10 18:01:54 EDT 2024
Thu Sep 12 19:42:59 EDT 2024
Sat Sep 28 07:49:02 EDT 2024
Sun Oct 22 16:08:59 EDT 2023
Wed May 18 15:26:48 EDT 2016
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 15
Keywords Nucleotidyltransferases
Peptides
Enzyme
Transferases
Escherichia coli
Bacteria
Replication
DNA-directed DNA polymerase
Enterobacteriaceae
Language English
License CC BY 4.0
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c464t-c2248ba199b0d4002a4b98ddc08571cd6efdd445eb16356e85fb506e0e1f7d893
OpenAccessLink https://jb.asm.org/content/jb/193/15/3815.full.pdf
PMID 21622737
PQID 879336099
PQPubID 40724
PageCount 7
ParticipantIDs proquest_journals_879336099
pascalfrancis_primary_24404536
crossref_primary_10_1128_JB_01550_10
pubmed_primary_21622737
pubmedcentral_primary_oai_pubmedcentral_nih_gov_3147505
highwire_asm_jb_193_15_3815
PublicationCentury 2000
PublicationDate 2011-08-01
PublicationDateYYYYMMDD 2011-08-01
PublicationDate_xml – month: 08
  year: 2011
  text: 2011-08-01
  day: 01
PublicationDecade 2010
PublicationPlace Washington, DC
PublicationPlace_xml – name: Washington, DC
– name: United States
– name: Washington
– name: 1752 N St., N.W., Washington, DC
PublicationTitle Journal of Bacteriology
PublicationTitleAlternate J Bacteriol
PublicationYear 2011
Publisher American Society for Microbiology
Publisher_xml – name: American Society for Microbiology
References 17868748 - Mutat Res. 2008 Jan 1;637(1-2):161-72
19019142 - Mol Microbiol. 2009 Jan;71(2):315-31
19397281 - Chem Res Toxicol. 2009 May;22(5):759-78
9665722 - Biochemistry. 1998 Jul 14;37(28):10164-72
10801133 - Nature. 2000 Apr 27;404(6781):1014-8
1550814 - Biochemistry. 1992 Mar 24;31(11):2879-86
15795165 - Mutat Res. 2005 Mar;589(2):111-35
18788757 - Chem Res Toxicol. 2008 Oct;21(10):1983-90
10813660 - Chem Res Toxicol. 2000 May;13(5):421-9
7012155 - J Biol Chem. 1981 May 10;256(9):4676-8
20523737 - PLoS One. 2010;5(5):e10862
11352575 - J Mol Biol. 2001 May 18;308(5):823-37
11101526 - EMBO J. 2000 Dec 1;19(23):6536-45
2040637 - J Biol Chem. 1991 Jun 15;266(17):11328-34
7768936 - J Biol Chem. 1995 Jun 2;270(22):13348-57
12097328 - J Biol Chem. 2002 Sep 13;277(37):34198-207
15779911 - Biochemistry. 2005 Mar 29;44(12):4850-60
16230118 - Adv Protein Chem. 2005;71:401-40
20604523 - Biochemistry. 2010 Jul 27;49(29):6155-64
9079893 - J Bacteriol. 1997 Apr;179(7):2109-15
15723543 - Biochemistry. 2005 Mar 1;44(8):3000-9
11842222 - Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1905-9
12060704 - Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8737-41
1534562 - J Biol Chem. 1992 Jun 5;267(16):11431-8
12502710 - J Biol Chem. 2003 Feb 21;278(8):5970-6
12045089 - Annu Rev Biochem. 2002;71:17-50
7753632 - Nucleic Acids Res. 1995 Apr 25;23(8):1398-405
7578929 - Chem Res Toxicol. 1995 Apr-May;8(3):422-30
20102227 - Chem Res Toxicol. 2010 Mar 15;23(3):689-95
7681219 - Science. 1993 Mar 19;259(5102):1757-60
8631887 - J Biol Chem. 1996 May 3;271(18):10767-74
9618448 - Microbiol Mol Biol Rev. 1998 Jun;62(2):434-64
8594343 - Methods Enzymol. 1995;262:13-21
Minko I. G. (e_1_3_2_20_2) 2008; 637
Pritchard A. E. (e_1_3_2_27_2) 2000; 19
Rothwell P. J. (e_1_3_2_28_2) 2005; 71
Bonner C. A. (e_1_3_2_3_2) 1992; 267
Hastings P. J. (e_1_3_2_12_2) 2010; 5
Tang M. (e_1_3_2_30_2) 2000; 404
Cai H. (e_1_3_2_5_2) 1995; 262
Yadav P. N. (e_1_3_2_31_2) 1992; 31
Minko I. G. (e_1_3_2_19_2) 2009; 22
Cox M. M. (e_1_3_2_7_2) 1981; 256
Fernandes A. (e_1_3_2_10_2) 1998; 37
Latham G. J. (e_1_3_2_18_2) 1995; 8
Chary P. (e_1_3_2_6_2) 1995; 23
Yamanaka K. (e_1_3_2_32_2) 2010; 23
Stukenberg P. T. (e_1_3_2_29_2) 1991; 266
e_1_3_2_9_2
e_1_3_2_16_2
Minko I. G. (e_1_3_2_23_2) 2002; 99
Bruck I. (e_1_3_2_4_2) 1996; 271
Goodman M. F (e_1_3_2_11_2) 2002; 71
Patel P. H. (e_1_3_2_26_2) 2001; 308
Minko I. G. (e_1_3_2_21_2) 2005; 44
Barker S. (e_1_3_2_2_2) 2005; 589
Kobayashi S. (e_1_3_2_15_2) 2002; 277
e_1_3_2_34_2
Yeiser B. (e_1_3_2_33_2) 2002; 99
Nechev L. V. (e_1_3_2_24_2) 2000; 13
Minko I. G. (e_1_3_2_22_2) 2008; 21
Onrust R. (e_1_3_2_25_2) 1995; 270
Hwang H. (e_1_3_2_14_2) 2005; 44
Curti E. (e_1_3_2_8_2) 2009; 71
Huang H. (e_1_3_2_13_2) 2010; 49
Kurtz A. J. (e_1_3_2_17_2) 2003; 278
References_xml – volume: 256
  start-page: 4676
  year: 1981
  ident: e_1_3_2_7_2
  article-title: A simple and rapid procedure for the large scale purification of the recA protein of Escherichia coli
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)69488-3
  contributor:
    fullname: Cox M. M.
– volume: 637
  start-page: 161
  year: 2008
  ident: e_1_3_2_20_2
  article-title: Mutagenic potential of DNA-peptide crosslinks mediated by acrolein-derived DNA adducts
  publication-title: Mutat. Res.
  doi: 10.1016/j.mrfmmm.2007.08.001
  contributor:
    fullname: Minko I. G.
– volume: 21
  start-page: 1983
  year: 2008
  ident: e_1_3_2_22_2
  article-title: Replication bypass of the acrolein-mediated deoxyguanine DNA-peptide cross-links by DNA polymerases of the DinB family
  publication-title: Chem. Res. Toxicol.
  doi: 10.1021/tx800174a
  contributor:
    fullname: Minko I. G.
– volume: 8
  start-page: 422
  year: 1995
  ident: e_1_3_2_18_2
  article-title: The efficiency of translesion synthesis past single styrene oxide DNA adducts in vitro is polymerase-specific
  publication-title: Chem. Res. Toxicol.
  doi: 10.1021/tx00045a014
  contributor:
    fullname: Latham G. J.
– volume: 278
  start-page: 5970
  year: 2003
  ident: e_1_3_2_17_2
  article-title: 1,N 2-Deoxyguanosine adducts of acrolein, crotonaldehyde, and trans-4-hydroxynonenal cross-link to peptides via Schiff base linkage
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M212012200
  contributor:
    fullname: Kurtz A. J.
– volume: 267
  start-page: 11431
  year: 1992
  ident: e_1_3_2_3_2
  article-title: Processive DNA synthesis by DNA polymerase II mediated by DNA polymerase III accessory proteins
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)49928-6
  contributor:
    fullname: Bonner C. A.
– volume: 262
  start-page: 13
  year: 1995
  ident: e_1_3_2_5_2
  article-title: Purification and properties of DNA polymerase II from Escherichia coli
  publication-title: Methods Enzymol.
  doi: 10.1016/0076-6879(95)62004-4
  contributor:
    fullname: Cai H.
– volume: 22
  start-page: 759
  year: 2009
  ident: e_1_3_2_19_2
  article-title: Chemistry and biology of DNA containing 1,N 2-deoxyguanosine adducts of the alpha, beta-unsaturated aldehydes acrolein, crotonaldehyde, and 4-hydroxynonenal
  publication-title: Chem. Res. Toxicol.
  doi: 10.1021/tx9000489
  contributor:
    fullname: Minko I. G.
– volume: 37
  start-page: 10164
  year: 1998
  ident: e_1_3_2_10_2
  article-title: Mutagenic potential of stereoisomeric bay region (+)- and (−)-cis-anti-benzo[a]pyrene diol epoxide-N 2-2′-deoxyguanosine adducts in Escherichia coli and simian kidney cells
  publication-title: Biochemistry
  doi: 10.1021/bi980401f
  contributor:
    fullname: Fernandes A.
– volume: 271
  start-page: 10767
  year: 1996
  ident: e_1_3_2_4_2
  article-title: Purification of a soluble UmuD′C complex from Escherichia coli. Cooperative binding of UmuD′C to single-stranded DNA
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.271.18.10767
  contributor:
    fullname: Bruck I.
– volume: 71
  start-page: 401
  year: 2005
  ident: e_1_3_2_28_2
  article-title: Structure and mechanism of DNA polymerases
  publication-title: Adv. Protein Chem.
  doi: 10.1016/S0065-3233(04)71011-6
  contributor:
    fullname: Rothwell P. J.
– volume: 71
  start-page: 315
  year: 2009
  ident: e_1_3_2_8_2
  article-title: DNA polymerase switching: effects on spontaneous mutagenesis in Escherichia coli
  publication-title: Microbiol. Mol. Biol. Rev.
  contributor:
    fullname: Curti E.
– volume: 49
  start-page: 6155
  year: 2010
  ident: e_1_3_2_13_2
  article-title: Minor groove orientation of the KWKK peptide tethered via the N-terminal amine to the acrolein-derived 1, N 2-γ-hydroxypropanodeoxyguanosine lesion with a trimethylene linkage
  publication-title: Biochemistry
  doi: 10.1021/bi100364f
  contributor:
    fullname: Huang H.
– volume: 44
  start-page: 4850
  year: 2005
  ident: e_1_3_2_14_2
  article-title: Evidence for Watson-Crick and not Hoogsteen or wobble base pairing in the selection of nucleotides for insertion opposite pyrimidines and a thymine dimer by yeast DNA pol η
  publication-title: Biochemistry
  doi: 10.1021/bi048244+
  contributor:
    fullname: Hwang H.
– volume: 19
  start-page: 6536
  year: 2000
  ident: e_1_3_2_27_2
  article-title: A novel assembly mechanism for the DNA polymerase III holoenzyme DnaX complex: association of δδ′ with DnaX4 forms DnaX3 δδ′
  publication-title: EMBO J.
  doi: 10.1093/emboj/19.23.6536
  contributor:
    fullname: Pritchard A. E.
– volume: 266
  start-page: 11328
  year: 1991
  ident: e_1_3_2_29_2
  article-title: Mechanism of the sliding β-clamp of DNA polymerase III holoenzyme
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)99166-0
  contributor:
    fullname: Stukenberg P. T.
– volume: 308
  start-page: 823
  year: 2001
  ident: e_1_3_2_26_2
  article-title: Prokaryotic DNA polymerase I: evolution, structure, and “base flipping” mechanism for nucleotide selection
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.2001.4619
  contributor:
    fullname: Patel P. H.
– volume: 71
  start-page: 17
  year: 2002
  ident: e_1_3_2_11_2
  article-title: Error-prone repair DNA polymerases in prokaryotes and eukaryotes
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.71.083101.124707
  contributor:
    fullname: Goodman M. F
– volume: 277
  start-page: 34198
  year: 2002
  ident: e_1_3_2_15_2
  article-title: Fidelity of Escherichia coli DNA polymerase IV. Preferential generation of small deletion mutations by dNTP-stabilized misalignment
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M204826200
  contributor:
    fullname: Kobayashi S.
– volume: 44
  start-page: 3000
  year: 2005
  ident: e_1_3_2_21_2
  article-title: Initiation of repair of DNA-polypeptide cross-links by the UvrABC nuclease
  publication-title: Biochemistry
  doi: 10.1021/bi0478805
  contributor:
    fullname: Minko I. G.
– volume: 99
  start-page: 1905
  year: 2002
  ident: e_1_3_2_23_2
  article-title: Incision of DNA-protein crosslinks by UvrABC nuclease suggests a potential repair pathway involving nucleotide excision repair
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.042700399
  contributor:
    fullname: Minko I. G.
– volume: 589
  start-page: 111
  year: 2005
  ident: e_1_3_2_2_2
  article-title: DNA-protein crosslinks: their induction, repair, and biological consequences
  publication-title: Mutat. Res.
  doi: 10.1016/j.mrrev.2004.11.003
  contributor:
    fullname: Barker S.
– volume: 5
  start-page: e10862
  year: 2010
  ident: e_1_3_2_12_2
  article-title: Competition of Escherichia coli DNA polymerases I, II and III with DNA Pol IV in stressed cells
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0010862
  contributor:
    fullname: Hastings P. J.
– volume: 270
  start-page: 13348
  year: 1995
  ident: e_1_3_2_25_2
  article-title: Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. I. Organization of the clamp loader
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.270.22.13348
  contributor:
    fullname: Onrust R.
– ident: e_1_3_2_16_2
  doi: 10.1128/jb.179.7.2109-2115.1997
– volume: 23
  start-page: 1398
  year: 1995
  ident: e_1_3_2_6_2
  article-title: In vitro replication by prokaryotic and eukaryotic polymerases on DNA templates containing site-specific and stereospecific benzo[a]pyrene-7,8-dihydrodiol-9,10-epoxide adducts
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/23.8.1398
  contributor:
    fullname: Chary P.
– volume: 13
  start-page: 421
  year: 2000
  ident: e_1_3_2_24_2
  article-title: Synthesis of nucleosides and oligonucleotides containing adducts of acrolein and vinyl chloride
  publication-title: Chem. Res. Toxicol.
  doi: 10.1021/tx990167+
  contributor:
    fullname: Nechev L. V.
– volume: 404
  start-page: 1014
  year: 2000
  ident: e_1_3_2_30_2
  article-title: Roles of E. coli DNA polymerases IV and V in lesion-targeted and untargeted SOS mutagenesis
  publication-title: Nature
  doi: 10.1038/35010020
  contributor:
    fullname: Tang M.
– volume: 99
  start-page: 8737
  year: 2002
  ident: e_1_3_2_33_2
  article-title: SOS-induced DNA polymerases enhance long-term survival and evolutionary fitness
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.092269199
  contributor:
    fullname: Yeiser B.
– volume: 31
  start-page: 2879
  year: 1992
  ident: e_1_3_2_31_2
  article-title: A molecular model of the complete three-dimensional structure of the Klenow fragment of Escherichia coli DNA polymerase I: binding of the dNTP substrate and template-primer
  publication-title: Biochemistry
  doi: 10.1021/bi00126a006
  contributor:
    fullname: Yadav P. N.
– ident: e_1_3_2_34_2
  doi: 10.1126/science.7681219
– ident: e_1_3_2_9_2
  doi: 10.1128/MMBR.62.2.434-464.1998
– volume: 23
  start-page: 689
  year: 2010
  ident: e_1_3_2_32_2
  article-title: Novel enzymatic function of DNA polymerase ν in translesion DNA synthesis past major groove DNA-peptide and DNA-DNA cross-links
  publication-title: Chem. Res. Toxicol.
  doi: 10.1021/tx900449u
  contributor:
    fullname: Yamanaka K.
SSID ssj0014452
Score 2.1643388
Snippet Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
Reaction of bifunctional electrophiles with DNA in the presence of peptides can result in DNA-peptide cross-links. In particular, the linkage can be formed in...
ABSTRACT Reaction of bifunctional electrophiles with DNA in the presence of peptides can result in DNA-peptide cross-links. In particular, the linkage can be...
SourceID pubmedcentral
proquest
crossref
pubmed
pascalfrancis
highwire
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 3815
SubjectTerms Bacteriology
Biological and medical sciences
Cells
Cross-Linking Reagents - chemistry
Deoxyadenosines - chemistry
Deoxyadenosines - genetics
DNA Adducts - chemistry
DNA Adducts - genetics
DNA Damage
DNA Polymerase I - genetics
DNA Polymerase I - metabolism
DNA Repair
DNA Replication
DNA, Bacterial - chemistry
DNA, Bacterial - genetics
DNA, Single-Stranded - genetics
E coli
Escherichia coli - enzymology
Escherichia coli - genetics
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Fundamental and applied biological sciences. Psychology
Genetics and Molecular Biology
Microbiology
Miscellaneous
Peptides
Peptides - chemistry
Title Role of High-Fidelity Escherichia coli DNA Polymerase I in Replication Bypass of a Deoxyadenosine DNA-Peptide Cross-Link
URI http://jb.asm.org/content/193/15/3815.abstract
https://www.ncbi.nlm.nih.gov/pubmed/21622737
https://www.proquest.com/docview/879336099
https://pubmed.ncbi.nlm.nih.gov/PMC3147505
Volume 193
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3Pa9swFH60hcEuY91Pr13QoVcltiPJ9rFJG9qMljBW6E1IlsQ8ErvUGTT__Z5sq1vGTrvalrD1vR-f5KdPAGfWYiJQ6EgqSR1lmXZUx0VJRWzKjIscM4bfjXxzK67u2PKe3x8AD3thuqL9Ulfjer0Z19X3rrbyYVNOQp3YZHUznyYMEx2fHMIhGmiYog-_Dhjjg0R4gp5cTIdNeRiHJ8vZuKPkGHs6EWCRYvLO9jNSUAn2RZKqxXFy_QEX_2KgfxdS_pGZFq_h1UApyXn_6sdwYOs38KI_ZHL3Fp6-NmtLGkd8SQddeFkrZN7ksvVwVb7UmaAxVOTi9pysmvXOr1K1llyTqiZIz8OiHpnt8E1b35EiF7Z52injhcaRpfqmdOXLY4wlc_-R1E9x38Hd4vLb_IoO5y3Qkgm2pSWm81yrpCh0bNC3U8V0kRtTehX8pDTCOmNweDG8e1U7m3OneSxsbBOXGSQ-7-Gobmr7EUiRa4dkgitkH0xlTiGzUsgmLWcqT7WL4CyMuXzoZTVkNx1Jc7mcyQ4lvBDBScBDqnYjf2iJiMqESyQaPILRHkTPPaVe9JBPBTYPmMnBNVuZY0SaCiTGEXzo0fvdbrCICLI9XJ8f8Frc-3fQRDtN7sEkP_13yxN4GZar4-QUjraPP-1n5DtbPUKmf_1l1Fn5L598_sk
link.rule.ids 230,315,730,783,787,888,27936,27937,53804,53806
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwFD4aQwheEHfCYPhhr26T1M7lce1WdWWtKrRJe7Ps2BZBbTKRTlr__Y6TeFDEE69JbCX-zuWzc_wZ4MQYTAQSHUlGsaUsVZaqMC9oEuoi5UmGGcPtRl4sk9k1m9_wmwPgfi9MW7RfqHJQrTeDqvzR1lbeboqhrxMbrhaTUcQw0fHhE3iK_hoyP0nvfx4wxnuR8Ah9OR_12_IwEg_n40FLyjH6tDLASYzpO93PSV4n2JVJygZHynZHXPyLg_5dSvlHbpq-gpc9qSSn3cu_hgNTvYFn3TGTu7dw_71eG1Jb4oo66NQJWyH3JueNA6x0xc4EzaEkZ8tTsqrXO7dO1RhyQcqKIEH3y3pkvMM3bVxHkpyZ-n4ntZMaR57qmtKVK5DRhkzcR1I3yX0H19Pzq8mM9icu0IIlbEsLTOiZklGeq1Cjd8eSqTzTunA6-FGhE2O1xuHFAO907UzGreJhYkIT2VQj9XkPh1VdmY9A8kxZpBNcIv9gMrUSuZVEPmk4k1msbAAnfszFbSesIdoJSZyJ-Vi0KOGFAI48HkI2G_FTCURURFwg1eABHO9B9NhT7GQP-SjB5h4z0TtnIzKMSaMEqXEAHzr0frfrLSKAdA_XxwecGvf-HTTSVpW7N8pP_93yKzyfXS0uxeXF8tsRvPCL12H0GQ63v-7MF2Q_W3Xc2voDLjcBNQ
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwFD6CIRAviDthMPywVzeX2k7yuLartsKqCjFpb5Yd2yKoTSpSpPXfc5zLWBFPvCY5VuJz--wcfwfg1FpMBAodScWJoyzVjuooL6iITJFykWHG8KeRr5bi4potbvjNvVZfbdF-octRtd6MqvJ7W1u53RThUCcWrq6m45hhouPh1rjwITxCn43EsFDvfyAwxnui8Bj9OR_3R_MwGoeLyagF5hiBWipgkWAKTw_z0sAV7EslVYOz5bo2F__CoX-XU97LT_Pn8KwHluSs-4AX8MBWL-Fx12py_wpuv9ZrS2pHfGEHnXtyK8Tf5LzxSit9wTNBkyjJbHlGVvV67_eqGksuSVkRBOnD1h6Z7PFNGz-QIjNb3-6V8XTjiFW9KF35IhljydR_JPUL3ddwPT__Nr2gfdcFWjDBdrTApJ5pFee5jgx6eKKYzjNjCs-FHxdGWGcMTi8Gec9tZzPuNI-EjWzsUoPw5w0cVXVl3wHJM-0QUnCFGISp1CnEVwoxpeVMZYl2AZwOcy63HbmGbBclSSYXE9lqCS8EcDzoQ6pmI39oiRqVMZcIN3gAJwcquhsp8dSHfCxQfNCZ7B20kRnGpbFAeBzA2057f-R6iwggPdDr3QOekfvwDhpqy8zdG-b7_5b8BE9Ws7n8crn8fAxPh_3rKP4AR7ufv-xHBEA7fdKa-m_p3wJI
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Role+of+High-Fidelity+Escherichia+coli+DNA+Polymerase+I+in+Replication+Bypass+of+a+Deoxyadenosine+DNA-Peptide+Cross-Link&rft.jtitle=Journal+of+Bacteriology&rft.au=Kinrin+Yamanaka&rft.au=Irina+G.+Minko&rft.au=Steven+E.+Finkel&rft.au=Myron+F.+Goodman&rft.date=2011-08-01&rft.pub=American+Society+for+Microbiology&rft.issn=0021-9193&rft.eissn=1067-8832&rft.volume=193&rft.issue=15&rft.spage=3815&rft_id=info:doi/10.1128%2FJB.01550-10&rft_id=info%3Apmid%2F21622737&rft.externalDBID=n%2Fa&rft.externalDocID=jb_193_15_3815
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0021-9193&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0021-9193&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0021-9193&client=summon